1jlt
From Proteopedia
(New page: 200px<br /><applet load="1jlt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jlt, resolution 1.4Å" /> '''Vipoxin Complex'''<br...) |
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| - | [[Image:1jlt.gif|left|200px]]<br /><applet load="1jlt" size=" | + | [[Image:1jlt.gif|left|200px]]<br /><applet load="1jlt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jlt, resolution 1.4Å" /> | caption="1jlt, resolution 1.4Å" /> | ||
'''Vipoxin Complex'''<br /> | '''Vipoxin Complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Vipoxin is a neurotoxic postsynaptic heterodimeric complex from the venom | + | Vipoxin is a neurotoxic postsynaptic heterodimeric complex from the venom of Vipera ammodytes meridionalis, the most toxic snake in Europe. It consists of a basic and highly toxic phospholipase A(2) and an acidic non-toxic protein inhibitor. The two polypeptide chains have the same chain length and share 62% amino-acid identity. Vipoxin is a unique example of evolution of the catalytic and toxic phospholipase A(2) functions into inhibitory and non-toxic functions. The crystal structure of the complex has been determined by the molecular-replacement method and refined to 1.4 A resolution to an R factor of 18.2%. The complex formation decreases the accessible surface area of the two subunits by approximately 1480 A(2), which results in a reduction of toxicity and catalytic activity. The catalytic and substrate-binding sites of the vipoxin phospholipase A(2) are identical or similar to those of other group I/II enzymes. Two 2-methyl-2,4-pentanediol molecules are present in the hydrophobic channel close to the active site. The two subunits lack calcium ions. The negatively charged Asp49 of the phospholipase A(2), which participates in the Ca(2+)-binding sites of other snake-venom phospholipase A(2)s, is neutralized by the side chain of Lys69 from the inhibitor. Attempts have been made to identify the toxicity region and to explain the reduced catalytic activity and toxicity of the phospholipase A(2) subunit. |
==About this Structure== | ==About this Structure== | ||
| - | 1JLT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vipera_ammodytes_ammodytes Vipera ammodytes ammodytes] with MRD and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http:// | + | 1JLT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vipera_ammodytes_ammodytes Vipera ammodytes ammodytes] with <scene name='pdbligand=MRD:'>MRD</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JLT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Genov, N.]] | [[Category: Genov, N.]] | ||
[[Category: Notzel, C.]] | [[Category: Notzel, C.]] | ||
| - | [[Category: Rajashankar, K | + | [[Category: Rajashankar, K R.]] |
| - | [[Category: Singh, T | + | [[Category: Singh, T P.]] |
[[Category: MPD]] | [[Category: MPD]] | ||
[[Category: MRD]] | [[Category: MRD]] | ||
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[[Category: vipoxin]] | [[Category: vipoxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:06 2008'' |
Revision as of 11:24, 21 February 2008
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Vipoxin Complex
Overview
Vipoxin is a neurotoxic postsynaptic heterodimeric complex from the venom of Vipera ammodytes meridionalis, the most toxic snake in Europe. It consists of a basic and highly toxic phospholipase A(2) and an acidic non-toxic protein inhibitor. The two polypeptide chains have the same chain length and share 62% amino-acid identity. Vipoxin is a unique example of evolution of the catalytic and toxic phospholipase A(2) functions into inhibitory and non-toxic functions. The crystal structure of the complex has been determined by the molecular-replacement method and refined to 1.4 A resolution to an R factor of 18.2%. The complex formation decreases the accessible surface area of the two subunits by approximately 1480 A(2), which results in a reduction of toxicity and catalytic activity. The catalytic and substrate-binding sites of the vipoxin phospholipase A(2) are identical or similar to those of other group I/II enzymes. Two 2-methyl-2,4-pentanediol molecules are present in the hydrophobic channel close to the active site. The two subunits lack calcium ions. The negatively charged Asp49 of the phospholipase A(2), which participates in the Ca(2+)-binding sites of other snake-venom phospholipase A(2)s, is neutralized by the side chain of Lys69 from the inhibitor. Attempts have been made to identify the toxicity region and to explain the reduced catalytic activity and toxicity of the phospholipase A(2) subunit.
About this Structure
1JLT is a Protein complex structure of sequences from Vipera ammodytes ammodytes with and as ligands. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.
Reference
Structure of the neurotoxic complex vipoxin at 1.4 A resolution., Banumathi S, Rajashankar KR, Notzel C, Aleksiev B, Singh TP, Genov N, Betzel C, Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1552-9. Epub 2001, Oct 25. PMID:11679719
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